We are: (1) utilizing methods to purify vWF free of AHF (10,000 X purified); making AHF free of vWF and purified about 200,000 times; refining the technique of analytical ultrafiltration; (2) developing further a micro method for N-terminal analysis and employing it and polyacrylamide gels to analyze the highly purified fibrinogen-fibrin related antigen from patients with defibrination or cirrhosis of the liver; (3) extending our recently developed procedure for binding ligands to solid-phase matrices for affinity chromatography and providing the necessary chemical control to optimize activation of the matrices and binding of specific amounts of ligand for various purposes; immobilizing sulfhydryl compounds for thiol-exchange chromatography of AHF; (4) studying further the binding of proteins by solid-phase polyelectrolytes; and (5) attempting to isolate the receptor for fibrinogen which is induced on platelets when they are exposed to ADP; studying the size of the AHF molecule in BaSO4-adsorbed native plasma, and the ability of AHF (a) to function in coagulation in the absence of von Willebrand factor, and (b) to bind to platelets.